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KMID : 0811720110150040245
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Korean Journal of Physiology & Pharmacology
2011 Volume.15 No. 4 p.245 ~ p.249
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Amphetamine-induced ERM Proteins Phosphorylation Is through PKCb Activation in PC12 Cells
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Jeong Ha-Jin
Jeon Song-Hee
Kim Jeong-Hoon
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Abstract
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Amphetamine, a synthetic psychostimulant, is transported by the dopamine transporter (DAT) to the cytosol and increases the exchange of extracellular amphetamine by intracellular dopamine. Recently, we reported that the phosphorylation levels of ezrin-radixin-moesin (ERM) proteins are regulated by psychostimulant drugs in the nucleus accumbens, a brain area important for drug addiction. However, the significance of ERM proteins phosphorylation in response to drugs of abuse has not been fully investigated. In this study, using PC12 cells as an in vitro cell model, we showed that amphetamine increases ERM proteins phosphorylation and protein kinase C (PKC) b inhibitor, but not extracellular signal-regulated kinase (ERK) or phosphatidylinositol 3-kinases (PI3K) inhibitors, abolished this effect. Further, we observed that DAT inhibitor suppressed amphetamine-induced ERM proteins phosphorylation in PC12 cells. These results suggest that PKCb-induced DAT regulation may be involved in amphetmaine-induced ERM proteins phosphorylation.
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KEYWORD
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Amphetamine, ERM proteins (ezrin, radixin, moesin), PKCb, PC12 cells, Dopamine transporter
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